MolNFT v1 · #165154 · protein
Structure of methylene-tetrahydromethanopterin dehydrogenase from methylorubrum extorquens AM1 in an open conformation containing NADP+ and methylene-H4MPT
6TLK: “Structure of methylene-tetrahydromethanopterin dehydrogenase from methylorubrum extorquens AM1 in an open…”. X-ray diffraction, 4 ligands (NAP, H4M, MG). MolNFT v1 #165154 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 6TLK
- Type
- protein
- Length
- 1,729 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P55818
- Ligands
- NAP, H4M, MG, CL
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 289 | — | P55818 |
| B, C, D, E, F | — | protein | 288 | — | P55818 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 6 copies · chains A, B, C, D, E, F
- H4M · 5,10-dimethylene tetrahydromethanopterin · ligand · 2 copies · chains A, C, B
- MG · Magnesium ion · metal
- CL · Chloride ion · ion · chains D, E, F
- FMT · Formic acid · additive · 13 copies · chains A, D, C, B, E, F
- GOL · Glycerol · additive · 6 copies · chains C, A, E, F, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6TLK · Structure of methylene-tetrahydromethanopterin dehydrogenase from Methylorubrum… · the same entry in another collection · chain F against F, TM-score 1.00
- P55818 · AlphaFold monomer V2.0 prediction for bifunctional protein mdta (P55818) · a predicted model of the same protein · chain A against A, TM-score 0.99
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P55818
- Elsewhere: RCSB PDB 6TLK · PDBe 6TLK · UniProt P55818
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